Interfacial and foaming properties of enzyme-induced hydrolysis of sunflower protein isolate

Patino, Juan M. Rodrı́guez; Conde, José Miñones; Linares, Herminia Millán; Jiménez, Justo J. Pedroche; Sánchez, Cecilio Carrera; Pizones, Víctor Manuel; Rodríguez, Francisco Millán

doi:10.1016/j.foodhyd.2006.09.002

Cited by 85 publications

(24 citation statements)

References 46 publications

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“…These results show the complexity of variables leading to increase or decrease the overall foam stability. Some authors [20] have been demonstrated that the foam stability increased with protein concentration in solution as can be seen in the current work. These results were also in agreement with the interfacial characteristics of the adsorbed films.…”

Section: Effects Of Hius On Stability Parameters Of Foamssupporting

confidence: 77%

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Improved Functionality of Foamed WPI Solutions by Ultrasound Application

Martínez¹,

Sánchez²

2016

J Food Chem Nanotechnol

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Section: Effects Of Hius On Stability Parameters Of Foamssupporting

confidence: 77%

“…Some authors found similar tendency [8,13,17,20]. It can be observed that HIUS effect on 2% WPI solution, depend on pH.…”

Section: Effect Of Hius On Bubbles Images Of Foamsmentioning

confidence: 55%

Improved Functionality of Foamed WPI Solutions by Ultrasound Application

Martínez¹,

Sánchez²

2016

J Food Chem Nanotechnol

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“…Indeed, for sunflower, soy, and wheat gluten protein, dynamic surface pressure measurements were indicative for FC, whereas FS could be linked to protein film elasticity (Conde and others , ; Rodriguez Patino and others ; Martínez and others ; Wouters and others ). Such thorough approach substantially contributed to a fundamental understanding of hydrolysate foaming properties and would be an asset when predicting foaming properties of plant protein hydrolysates in more complex real food systems.…”

Section: Functionality Of Plant Protein Hydrolysatesmentioning

confidence: 99%

Relevance of the Functional Properties of Enzymatic Plant Protein Hydrolysates in Food Systems

Wouters

Rombouts

Fierens

et al. 2016

Comp Rev Food Sci Food Safe

247

142

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Proteins play a crucial role in determining texture and structure of many food products. Although some animal proteins (such as egg white) have excellent functional and organoleptic properties, unfortunately, they entail a higher production cost and environmental impact than plant proteins. It is rather unfortunate that plant protein functionality is often insufficient because of low solubility in aqueous media. Enzymatic hydrolysis strongly increases solubility of proteins and alters their functional properties. The latter is attributed to 3 major structural changes: a decrease in average molecular mass, a higher availability of hydrophobic regions, and the liberation of ionizable groups. We here review current knowledge on solubility, water-and fat-holding capacity, gelation, foaming, and emulsifying properties of plant protein hydrolysates and discuss how these properties are affected by controlled enzymatic hydrolysis. In many cases, research in this field has been limited to fairly simple set-ups where functionality has been assessed in model systems. To evolve toward a more widely applied industrial use of plant protein hydrolysates, a more thorough understanding of functional properties is required. The structure-function relationship of protein hydrolysates needs to be studied in depth. Finally, test model systems closer to real food processing conditions, and thus to real foods, would be helpful to evaluate whether plant protein hydrolysates could be a viable alternative for other functional protein sources.

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“…Many studies have addressed the foaming properties of hydrolysed plant proteins on the basis of foaming capacity and foam stability, for example rice bran meal [12], bean (Phaseolus vulgaris L.) protein concentrates [13], rapeseed protein isolate [14], amaranth protein [15], Lupinus angustifolius protein [16], soy protein isolate [17] and pumpkin oil cake protein [18]. Yet, only a few studies have focused on the characterisation of the interfacial film of hydrolysed plant proteins and the effect of proteolysis on dynamic surface pressure measurements, in connection to foaming capacity and stability [19][20][21][22][23]. Interfacial rheology is a valuable tool for measuring the structural properties of proteins at interfaces.…”

Section: Introductionmentioning

confidence: 99%

Foaming characteristics of oat protein and modification by partial hydrolysis

Brückner-Gühmann

Heiden-Hecht

Sözer

et al. 2018

Eur Food Res Technol

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Foaming ability of oat protein isolate (OPI) was analysed at pH 4 and 7. Foaming properties were influenced by partial hydrolysis with trypsin (OPT) and alcalase (OPA). The viscoelasticity of the protein film, the interactions between the protein molecules, and the network forming within the protein film were analysed by interfacial rheology. At pH 7, foams made of OPI and OPT were found to be stable with OPI having the fastest foaming ability. At pH 4, the foaming properties of OPI were found to be poor due to limited solubility. The specific cleavage behaviour of trypsin improved the foaming properties, especially at pH 4, resulting in a homogenous foam structure, a fast foaming ability and a highly viscoelastic interfacial film. The formation of a thick steric protein layer at pH 7 and the formation of strong hydrophobic interactions at pH 4 were found to be the dominating foam stabilisation mechanisms. In conclusion, oat protein ingredients were developed with targeted functional properties.

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Interfacial and foaming properties of enzyme-induced hydrolysis of sunflower protein isolate

Cited by 85 publications

References 46 publications

Improved Functionality of Foamed WPI Solutions by Ultrasound Application

Improved Functionality of Foamed WPI Solutions by Ultrasound Application

Relevance of the Functional Properties of Enzymatic Plant Protein Hydrolysates in Food Systems

Foaming characteristics of oat protein and modification by partial hydrolysis

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